ID A0A2K5U8P9_MACFA Unreviewed; 1063 AA.
AC A0A2K5U8P9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000256|ARBA:ARBA00044109};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
GN Name=UBA1 {ECO:0000313|Ensembl:ENSMFAP00000008727.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000008727.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000008727.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000008727.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR AlphaFoldDB; A0A2K5U8P9; -.
DR STRING; 9541.ENSMFAP00000008727; -.
DR Ensembl; ENSMFAT00000021330.2; ENSMFAP00000008727.2; ENSMFAG00000001128.2.
DR VEuPathDB; HostDB:ENSMFAG00000001128; -.
DR GeneTree; ENSGT00940000158975; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000001128; Expressed in frontal cortex and 13 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF155; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 971..1056
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 51..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 683
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1063 AA; 117729 MW; C57F93EFA920A865 CRC64;
MSKPHFPPAL PPPAAVPGIK GEENGCLLLP TYSVPGSVLC VIYHLDNPMG KMSSSPLSKK
RRVSGPDPKP GSNCSPAQSV LSEVPSVPTN GMAKNGSEAD IDEGLYSRQL YVLGHEAMKR
LQTSSVLVSG LRGLGVEIAK NIILGGVKAV TLHDQGTAQW ADLSSQFYLR EEDIGKNRAE
VSQPRLAELN SYVPVTAYTG PLVEDFLSGF QVVVLTNTPL EDQLRVGEFC HSRGIKLVVA
DTRGLFGQLF CDFGKEMILT DSNGEQPLSA MVSMVTKDNP GVVTCLDEAR HGFESGDFVS
FSEVQGMVEL NGNQPMEIKV LGPYTFSICD TSNFSDYIRG GIVSQVKVPK KISFKSLVAS
LAEPDFVMTD FAKFSHPAQL HIGFQALHHF CAQHGRPPRP RNEEDATELV ALAQAVNARA
LPAVQQENLD EDLIRKLAYV AAGDLAPINA FIGGLAAQEV MKACSGKFMP IMQWLYFDAL
ECLPEDKEAL TEDKCLPRQN RYDGQVAVFG SDLQEKLGKQ KYFLVGAGAI GCELLKNFAM
IGLGCREGGE IIVTDMDTIE KSNLNRQFLF RPWDVTKLKS DTAAAAVRQM NPHIRVTSHQ
NRVGPDTERI YDDDFFQNLD GVANALDNVD ARMYMDRRCV YYRKPLLESG TLGTKGNVQV
VIPFLTESYS SSQDPPEKSI PICTLKNFPN AIEHTLQWAR DEFEGLFKQP AENVNQYLTD
PKFVERTLRL AGTQPLEVLE AVQRSLVLQR PQTWADCVTW ACHHWHTQYS NNIRQLLHNF
PPDQLTSSGA PFWSGPKRCP HPLTFDVNNP LHLDYVMAAA NLFAQTYGLT GSQDRAAVAT
LLQSVQVPEF TPKSGVKIHV SDQELQSANA SVDDSRLEEL KATLPSPDKL PGFKMYPIDF
EKDDDSNFHM DFIVAASNLR AENYDIPPAD RHKLIAGKII PAIATTTAAV VGLVCLELYK
VVQGHRQLDS YKNGFLNLAL PFFGFSEPLA APRHQYYNQE WTLWDRFEVQ GLQPNGDEMT
LKQFLDYFKT EHKLEITMLS QACPCSIPSS CQLPSSRNGW ISR
//